2OI5
E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000902 | biological_process | cell morphogenesis |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000902 | biological_process | cell morphogenesis |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 5000 |
| Chain | Residue |
| B | LYS25 |
| B | ASP105 |
| B | ASN227 |
| B | UD14001 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 5001 |
| Chain | Residue |
| B | ASP406 |
| B | ASP406 |
| B | ASP406 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 5002 |
| Chain | Residue |
| B | ASP406 |
| B | GLN408 |
| B | GLN408 |
| B | GLN408 |
| B | ASP406 |
| B | ASP406 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 5003 |
| Chain | Residue |
| A | ASP406 |
| A | ASP406 |
| A | ASP406 |
| A | MG5004 |
| A | MG5004 |
| A | MG5004 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MG A 5004 |
| Chain | Residue |
| A | ASP406 |
| A | ASP406 |
| A | ASP406 |
| A | MG5003 |
| A | MG5003 |
| A | MG5003 |
| A | HOH7207 |
| A | HOH7207 |
| A | HOH7207 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 6000 |
| Chain | Residue |
| A | ARG333 |
| A | LYS351 |
| A | HIS363 |
| A | TYR366 |
| A | ASN386 |
| A | LYS392 |
| A | HOH7262 |
| A | HOH7324 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 6001 |
| Chain | Residue |
| B | ARG333 |
| B | LYS351 |
| B | HIS363 |
| B | TYR366 |
| B | ASN386 |
| B | LYS392 |
| B | HOH7233 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 6002 |
| Chain | Residue |
| B | GLY16 |
| B | THR17 |
| B | ARG18 |
| B | UD14001 |
| B | HOH7219 |
| B | HOH7490 |
| B | HOH7513 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ACO A 2000 |
| Chain | Residue |
| A | TYR366 |
| A | GLY379 |
| A | ALA380 |
| A | THR384 |
| A | CYS385 |
| A | ASN386 |
| A | TYR387 |
| A | PHE402 |
| A | GLY404 |
| A | SER405 |
| A | ALA422 |
| A | ALA423 |
| A | ARG440 |
| A | LYS446 |
| A | TRP449 |
| A | HOH7010 |
| A | HOH7070 |
| A | HOH7129 |
| A | HOH7238 |
| A | HOH7284 |
| A | HOH7340 |
| A | HOH7499 |
| B | ARG429 |
| B | THR444 |
| B | HOH7482 |
| site_id | BC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE ACO B 2001 |
| Chain | Residue |
| B | HOH7488 |
| B | HOH7519 |
| B | HOH7528 |
| B | HOH7553 |
| B | HOH7567 |
| A | ARG429 |
| A | PRO442 |
| A | THR444 |
| A | HOH7400 |
| B | TYR366 |
| B | GLY379 |
| B | ALA380 |
| B | THR384 |
| B | CYS385 |
| B | ASN386 |
| B | TYR387 |
| B | PHE402 |
| B | GLY404 |
| B | SER405 |
| B | ALA422 |
| B | ALA423 |
| B | ARG440 |
| B | LYS446 |
| B | TRP449 |
| B | HOH7218 |
| B | HOH7235 |
| B | HOH7352 |
| B | HOH7353 |
| B | HOH7452 |
| site_id | BC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE UD1 A 4000 |
| Chain | Residue |
| A | LEU11 |
| A | ALA13 |
| A | GLY14 |
| A | GLN76 |
| A | GLN79 |
| A | LEU80 |
| A | GLY81 |
| A | THR82 |
| A | TYR103 |
| A | ASP105 |
| A | TYR139 |
| A | GLY140 |
| A | GLU154 |
| A | ASN169 |
| A | THR170 |
| A | TYR197 |
| A | ILE198 |
| A | THR199 |
| A | HOH7292 |
| A | HOH7295 |
| A | HOH7300 |
| A | HOH7314 |
| A | HOH7378 |
| A | HOH7416 |
| A | HOH7486 |
| site_id | BC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE UD1 B 4001 |
| Chain | Residue |
| B | LEU11 |
| B | ALA12 |
| B | ALA13 |
| B | GLY14 |
| B | ARG18 |
| B | LYS25 |
| B | GLN76 |
| B | GLN79 |
| B | LEU80 |
| B | GLY81 |
| B | THR82 |
| B | ALA85 |
| B | TYR103 |
| B | GLY104 |
| B | ASP105 |
| B | TYR139 |
| B | GLY140 |
| B | GLU154 |
| B | ASN169 |
| B | THR170 |
| B | TYR197 |
| B | THR199 |
| B | ASN227 |
| B | MG5000 |
| B | SO46002 |
| B | HOH7215 |
| B | HOH7224 |
| B | HOH7228 |
| B | HOH7230 |
Functional Information from PROSITE/UniProt
| site_id | PS00101 |
| Number of Residues | 29 |
| Details | HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsdTqLvapVtVGkgAtIAagTtVtrnV |
| Chain | Residue | Details |
| A | VAL403-VAL431 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Region: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555230","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OI5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| A | ASN386 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| B | ASN386 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| A | ARG18 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| B | ARG18 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 811 |
| Chain | Residue | Details |
| A | ARG18 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 811 |
| Chain | Residue | Details |
| B | ARG18 | electrostatic stabiliser |
